Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus.

Detalhes bibliográficos
Autor(a) principal: Mendonça, Madalena
Data de Publicação: 2023
Outros Autores: Vicente, Cláudia, Espada, Margarida
Tipo de documento: Artigo
Idioma: por
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10174/36142
Resumo: ShK domain-containing proteins are peptides found in different parasitic and venomous organisms. From a previous transcriptomic dataset from Bursaphelenchus xylophilus, a plant-endoparasitic nematode that infects forest tree species, we identified 96 transcripts potentially as ShK domain-containing proteins with unknown function in the nematode genome. This study aimed to characterize and explore the functional role of genes encoding ShK domain-containing proteins in B. xylophilus biology. We selected and functionally analyzed nine candidate genes specific from B. xylophilus. In situ hybridization revealed expression of one B. xylophilus ShK in the pharyngeal gland cells, suggesting their delivery into host cells. Most of the transcripts are highly expressed during infection and showed a significant upregulation in response to peroxide products compared to the nematode catalase enzymes. We reported for the first time, the potential involvement of ShK domain genes in oxidative stress, suggesting that these proteins may have an important role protecting or modulating the reactive oxygen species (ROS) activity of the host plant during parasitism.
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spelling Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus.molecular plant-nematode interactionparasitismpinewood nematodeShK domain-containing proteinoxidative stressShK domain-containing proteins are peptides found in different parasitic and venomous organisms. From a previous transcriptomic dataset from Bursaphelenchus xylophilus, a plant-endoparasitic nematode that infects forest tree species, we identified 96 transcripts potentially as ShK domain-containing proteins with unknown function in the nematode genome. This study aimed to characterize and explore the functional role of genes encoding ShK domain-containing proteins in B. xylophilus biology. We selected and functionally analyzed nine candidate genes specific from B. xylophilus. In situ hybridization revealed expression of one B. xylophilus ShK in the pharyngeal gland cells, suggesting their delivery into host cells. Most of the transcripts are highly expressed during infection and showed a significant upregulation in response to peroxide products compared to the nematode catalase enzymes. We reported for the first time, the potential involvement of ShK domain genes in oxidative stress, suggesting that these proteins may have an important role protecting or modulating the reactive oxygen species (ROS) activity of the host plant during parasitism.MDPI2024-01-18T10:51:16Z2024-01-182023-12-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10174/36142http://hdl.handle.net/10174/36142porMendonça, M., Vicente, C.S.L., Espada, M. Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus. 2023. pp:1-16. 10.20944/preprints202312.0388.v1https://www.preprints.org/manuscript/202312.0388/v1maria.silva@uevora.ptcvicente@uevora.ptmespada@uevora.pt581doi: 10.20944/preprints202312.0388.v1Mendonça, MadalenaVicente, CláudiaEspada, Margaridainfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-01-23T01:46:49Zoai:dspace.uevora.pt:10174/36142Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T01:56:33.129906Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus.
title Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus.
spellingShingle Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus.
Mendonça, Madalena
molecular plant-nematode interaction
parasitism
pinewood nematode
ShK domain-containing protein
oxidative stress
title_short Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus.
title_full Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus.
title_fullStr Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus.
title_full_unstemmed Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus.
title_sort Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus.
author Mendonça, Madalena
author_facet Mendonça, Madalena
Vicente, Cláudia
Espada, Margarida
author_role author
author2 Vicente, Cláudia
Espada, Margarida
author2_role author
author
dc.contributor.author.fl_str_mv Mendonça, Madalena
Vicente, Cláudia
Espada, Margarida
dc.subject.por.fl_str_mv molecular plant-nematode interaction
parasitism
pinewood nematode
ShK domain-containing protein
oxidative stress
topic molecular plant-nematode interaction
parasitism
pinewood nematode
ShK domain-containing protein
oxidative stress
description ShK domain-containing proteins are peptides found in different parasitic and venomous organisms. From a previous transcriptomic dataset from Bursaphelenchus xylophilus, a plant-endoparasitic nematode that infects forest tree species, we identified 96 transcripts potentially as ShK domain-containing proteins with unknown function in the nematode genome. This study aimed to characterize and explore the functional role of genes encoding ShK domain-containing proteins in B. xylophilus biology. We selected and functionally analyzed nine candidate genes specific from B. xylophilus. In situ hybridization revealed expression of one B. xylophilus ShK in the pharyngeal gland cells, suggesting their delivery into host cells. Most of the transcripts are highly expressed during infection and showed a significant upregulation in response to peroxide products compared to the nematode catalase enzymes. We reported for the first time, the potential involvement of ShK domain genes in oxidative stress, suggesting that these proteins may have an important role protecting or modulating the reactive oxygen species (ROS) activity of the host plant during parasitism.
publishDate 2023
dc.date.none.fl_str_mv 2023-12-01T00:00:00Z
2024-01-18T10:51:16Z
2024-01-18
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10174/36142
http://hdl.handle.net/10174/36142
url http://hdl.handle.net/10174/36142
dc.language.iso.fl_str_mv por
language por
dc.relation.none.fl_str_mv Mendonça, M., Vicente, C.S.L., Espada, M. Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus. 2023. pp:1-16. 10.20944/preprints202312.0388.v1
https://www.preprints.org/manuscript/202312.0388/v1
maria.silva@uevora.pt
cvicente@uevora.pt
mespada@uevora.pt
581
doi: 10.20944/preprints202312.0388.v1
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
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